Funds are requested (jointly to National Institutes of Health and National Science Foundation) for partial contributions toward purchase of a 14. 1 tesla (600 MHz for protons) Fourier transform nuclear magnetic resonance (FT/NMR) spectrometer, equipped with high-resolution probes, variable- temperature control, and a full range of two- and three-dimensional data acquisition, data reduction, and display capabilities. The instrument will be devoted mainly to primary and secondary core users for structural analysis and mechanistic studies of proteins/enzymes (alpha-lactalbumin, 14 kDa; sulfite reductase, 24 kDa; ribonuclease H, 17 kDa; high potential iron protein, 9.5 kDa; adenylate kinase, 21.7 kDa, phospholipase A2, 14 kDa; catalytic domain of leader peptidase, 28 kDa; and flavodoxin, 16 kDa), and some synthetic polypeptides from immunogenic and long range electron-transfer studies. The primary user group (L. J. Berliner, J. A. Cowan, M.-D. Tsai, and M. H. Zehfus) have NMR-oriented research programs; secondary users (R. E. Dalbey, P. T. P. Kaumaya, M. H. Klapper, and R. P. Swenson) will make use of NMR by means of collaboration with core users. The instrument will be housed at, and operated and maintained by the Campus Chemical Instrument Center (CCIC). The program Director, A. G. Marshall, is CCIC Director. He and his staff will assume responsibIlity for instrument installation, operation, and maintenance. Marshall will also chair the operating committee and advise and assist users from both the core group and the rest of the OSU biochemical research community for efficient use of the facility. The Ohio State University will provide the balance of capital funds for purchase of the instrument, as well as installation costs, salaries of permanent CCIC staff, and funds for long- term maintenance of the instrument. Costs of expendibles will be recovered from modest user operating fees.